CYSP_SCHMA
ID CYSP_SCHMA Reviewed; 340 AA.
AC P25792;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cathepsin B-like cysteine proteinase;
DE EC=3.4.22.-;
DE AltName: Full=Antigen Sm31;
DE Flags: Precursor;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2725581; DOI=10.1016/0166-6851(89)90025-x;
RA Klinkert M.-Q., Felleisen R., Link G., Ruppel A., Beck E.;
RT "Primary structures of Sm31/32 diagnostic proteins of Schistosoma mansoni
RT and their identification as proteases.";
RL Mol. Biochem. Parasitol. 33:113-122(1989).
CC -!- FUNCTION: Thiol protease. Has a role as a digestive enzyme.
CC -!- TISSUE SPECIFICITY: Intestine (gut).
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; M21309; AAA29865.1; -; mRNA.
DR AlphaFoldDB; P25792; -.
DR SMR; P25792; -.
DR STRING; 6183.Smp_103610.1; -.
DR MEROPS; C01.062; -.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_3_3_1; -.
DR SABIO-RK; P25792; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR012599; Propeptide_C1A.
DR Pfam; PF00112; Peptidase_C1; 1.
DR Pfam; PF08127; Propeptide_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Hydrolase; Protease; Reference proteome; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..88
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026172"
FT CHAIN 89..340
FT /note="Cathepsin B-like cysteine proteinase"
FT /id="PRO_0000026173"
FT ACT_SITE 117
FT /evidence="ECO:0000250"
FT ACT_SITE 287
FT /evidence="ECO:0000250"
FT ACT_SITE 307
FT /evidence="ECO:0000250"
FT DISULFID 102..131
FT /evidence="ECO:0000250"
FT DISULFID 114..158
FT /evidence="ECO:0000250"
FT DISULFID 150..216
FT /evidence="ECO:0000250"
FT DISULFID 151..154
FT /evidence="ECO:0000250"
FT DISULFID 187..220
FT /evidence="ECO:0000250"
FT DISULFID 195..206
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 38593 MW; 5891CCBE8F1F5341 CRC64;
MLTSILCIAS LITFLEAHIS VKNEKFEPLS DDIISYINEH PNAGWRAEKS NRFHSLDDAR
IQMGARREEP DLRRKRRPTV DHNDWNVEIP SNFDSRKKWP GCKSIATIRD QSRCGSCWSF
GAVEAMSDRS CIQSGGKQNV ELSAVDLLTC CESCGLGCEG GILGPAWDYW VKEGIVTASS
KENHTGCEPY PFPKCEHHTK GKYPPCGSKI YNTPRCKQTC QRKYKTPYTQ DKHRGKSSYN
VKNDEKAIQK EIMKYGPVEA SFTVYEDFLN YKSGIYKHIT GEALGGHAIR IIGWGVENKT
PYWLIANSWN EDWGENGYFR IVRGRDECSI ESEVIAGRIN
